Fibronectin‐Binding Proteins of a Human Oral Spirochete <i>Treponema denticola</i>

Umemoto, Toshihiko; Nakatani, Yoshihiro; Nakamura, Yoshinori; Namikawa, Isamu

doi:10.1111/j.1348-0421.1993.tb03182.x

Cited by 32 publications

(34 citation statements)

References 14 publications

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“…Its SDS-PAGE protein profile is very similar to the 52-kDa Pj described here. The 62-kDa Pa of T. pallidum ATCC 27087 and the 53-kDa Pk of T. denticola ATCC 33520 are also found to be their outer envelope proteins capable of binding to fibronectin (20,21,33,34). The cellular locations of the Pb, Pc, Pd, Pg, and Pi, each of which was not a single binding polypeptide in each strain, have not been determined at present because of limitations of the application of techniques similar to that described above.…”

Section: Discussionmentioning

confidence: 99%

“…Fibronectin, laminin, and collagen are extracellular matrix components which mediate the binding of some Gram-positive and Gramnegative bacteria to host cells (2,4,5,7,9,13,30,37). Recently, we have reported that the 53-kDa and 72-kDa outer envelope proteins of T. denticola ATCC 33520 can bind to fibronectin, suggesting that fibronectin may mediate adherence of this spirochete to gingival tissues in vivo (34).…”

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confidence: 99%

“…T. pallidum possesses 34,000-daltons (34-kDa) surface lipoprotein (29), and a human oral spirochete T. denticola has adherence-associated surface proteins (19,34,35). Axial flagella which initiate at subterminal ends of a spiral protoplasmic cylinder seem to work effectively as a locomotive apparatus through relatively viscous environments such as mucus and/or intracellular spaces (8,11,24), but do not usually project from the surface of the protoplasmic cell (25).…”

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confidence: 99%

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Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Umemoto

Namikawa

1994

Microbiology and Immunology

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The polypeptides of seven strains of human treponemes were investigated by immunoblot analysis for their binding to the human placental collagens and laminin. Of the treponemal polypeptides, eleven polypeptides, 45‐kDa, 49‐kDa, and 62‐kDa polypeptides from T. pallidum ATCC 27087, a 48‐kDa polypeptide from T. phagedenis biotype Reiter, 51‐kDa and 53‐kDa polypeptides from T. vincentii ATCC 35580, 30‐kDa, 53‐kDa and 63‐kDa polypeptides from T. socranskii subsp. buccale ATCC 35534, a 52‐kDa polypeptide from T. denticola ATCC 35405, and a 53‐kDa polypeptide from T. denticola ATCC 33520 possessed an ability to bind to the laminin, type I, III, IV, or V collagen. An intermediate‐sized human oral isolate strain G7201 did not possess any laminin‐ or collagen‐binding polypeptides. Immunoelectron microscopy using intact treponemal cells with a single collagen‐binding polypeptide and the corresponding antisera demonstrated that the 51‐kDa and 53‐kDa polypeptides from T. vincentii, the 53‐kDa polypeptide from T. socranskii subsp. buccale ATCC 35534 and the 52‐kDa polypeptide from T. denticola ATCC 35405, were outer envelope proteins.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Umemoto

Namikawa

1994

Microbiology and Immunology

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“…Specific attachment to the extracellular matrix (ECM) component fibronectin has been documented for many pathogenic bacteria, including the related spirochetes Borrelia burgdorferi (19,35), Leptospira interrogans (26), and Treponema denticola (8)(9)(10)49). Fibronectin is also likely to be involved in T. pallidum cytoadherence.…”

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Treponema pallidumFibronectin-Binding Proteins

et al. 2004

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Putative adhesins were predicted by computer analysis of the Treponema pallidum genome. Two treponemal proteins, Tp0155 and Tp0483, demonstrated specific attachment to fibronectin, blocked bacterial adherence to fibronectin-coated slides, and supported attachment of fibronectin-producing mammalian cells. These results suggest Tp0155 and Tp0483 are fibronectin-binding proteins mediating T. pallidum-host interactions.

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“…Previous studies focused on potential adhesins (37,47) and on spirochete surface proteins (21,52,66) or other cellular components (11,35) cytotoxic to eukaryotic cells. Studies of membrane-associated proteins of two distinct strains of T. denticola identified a 70-kDa protein having fibronectin (FN)-binding (67) or FN-, laminin-, and fibrinogen-binding (37) activity. This protein was distinct from the 53-kDa Msp pore-forming adhesin in these strains, which also bound FN (23,37,67).…”

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Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment

et al. 2000

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Proteins secreted or exported by Treponema denticola have been implicated as mediators of specific interactions between the spirochete and subgingival tissues in periodontal diseases. However, limited information is available on the ability of this peptidolytic organism to bind or transport soluble peptides present in the subgingival environment. A prominent 70-kDa protein was isolated from surface extracts of T. denticola ATCC 35405. A clone expressing a portion of the protein was identified in an Escherichia coli expression library of T. denticola DNA. DNA sequence analysis showed that the cloned gene encoded a peptide homologous to OppA, the solute binding protein of an ATP-binding cassette-type peptide transporter involved in peptide uptake and environmental signaling in a wide range of bacteria. Genes encoding OppB, -C, -D, and -F were identified directly downstream of oppA in T. denticola. OppA was present in representative strains of T. denticola and in Treponema vincentii but was not detected in Treponema pectinovorum or Treponema socranskii. Immunogold electron microscopy suggested that OppA was accessible to proteins at the surface of the spirochete. Native OppA bound soluble plasminogen and fibronectin but did not bind to immobilized substrates or epithelial cells. A T. denticola oppA mutant bound reduced amounts of soluble plasminogen, and plasminogen binding to the parent strain was inhibited by the lysine analog -aminocaproic acid. Binding of soluble host proteins by OppA may be important both for spirochete-host interactions in the subgingival environment and for uptake of peptide nutrients.Treponema denticola is recognized as one of several potential pathogens in acute and chronic forms of human periodontal disease (50,55,62), and closely related spirochetes have been identified in bovine digital dermatitis lesions (10). Likely virulence factors of oral spirochetes include the ability to attach to host tissue and other microorganisms, motility and chemotaxis, immunomodulation, production of toxic metabolic byproducts, and direct cytopathogenicity (reviewed in reference 22). In the case of periodontal diseases, bacterial factors that contribute to the overgrowth of subgingival microflora must also be considered as potential virulence factors. These could include, for instance, uptake systems for peptide nutrients present in a high concentration in the inflamed gingival sulcus. Characterization of these processes will aid in understanding the biology of this organism and may suggest targets for treatment or prophylaxis.T. denticola derives energy primarily from anaerobic degradation of peptides and amino acids (63). Nutrient requirements of this organism are complex (71), and the mechanisms of nutrient uptake are not well understood (12,27,28,61). Peptide uptake requires specific systems for the binding and transport of substrates across the bacterial cell envelope. Oligopeptide uptake systems, members of a superfamily of highly conserved ATP-binding cassette (ABC) transporters, have been described...

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Fibronectin‐Binding Proteins of a Human Oral Spirochete Treponema denticola

Cited by 32 publications

References 14 publications

Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Binding of Host‐Associated Treponeme Proteins to Collagens and Laminin: A Possible Mechanism of Spirochetal Adherence to Host Tissues

Treponema pallidumFibronectin-Binding Proteins

Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment

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